ID A0A0F0HMV2_9PSEU Unreviewed; 451 AA.
AC A0A0F0HMV2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KJK56869.1};
GN ORFNames=UK12_20125 {ECO:0000313|EMBL:KJK56869.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK56869.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK56869.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK56869.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJK56869.1}.
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DR EMBL; JYJF01000063; KJK56869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0HMV2; -.
DR PATRIC; fig|1427391.3.peg.6130; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000033409; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002792; TRAM_dom.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF01938; TRAM; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS50926; TRAM; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000033409};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT DOMAIN 19..80
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 311
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 335
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 451 AA; 48384 MW; A1784130A29CF878 CRC64;
MRAAKPARAE RTPKAPTGDS LVGERYEVEV GPVAHGGGHC VARHEGRVLF VRHTLPGERV
IAQVTEGTTT SRFLRADAVE ILEAAKERIP APCPFSGPGK CGGCDWQHVT PGGQRKLKGQ
VLTEQLAKLA GLTPAEAGWD GSVEPVGGKL PAGEVPAWRS RIQYAVDPET GKAGLRRHRS
HDIEPIDRCL IAAPGVTELG IEARDWPGVE TVEAIAASGS SDRQVVLTPR AGAQLPLVEL
DQPVSISRID EQGLFHRVHG RTFVRERAAG RTWRVSNGGF WQIHPEAPTT LVDAVLAGLD
PQWGEMALDL YCGVGLFAGA LADRVGEDGA VLGIESSKQA VVDARHNLAE VDNVRIECDK
VESLLPRTGI TSTDLIVLDP PRAGAGRETV AHLVGLEARR IAYVACDPAA LARDLAFFRE
GGYRPVSLRA FDLFPMTHHF ECVAILEPVG E
//